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Interhelical contacts are required for the helix bundle fold of apolipophorin III and its ability to interact with lipoproteins.
Apolipophorin-III (apoLp-III) from the insect, Manduca sexta, is a 166-residue exchangeable apolipoprotein that plays a critical role in the dynamics of plasma lipoprotein interconversions. Our previous work indicated that a 36-residue C-terminal peptide fragment, generated by cyanogen bromide diges...
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| Autores principales: | , , , |
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| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
Cold Spring Harbor Laboratory Press
1998
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2143903/ https://ncbi.nlm.nih.gov/pubmed/9521109 |
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